FZD5_HUMAN
ID FZD5_HUMAN Reviewed; 585 AA.
AC Q13467; A8K2X1; B2RCZ1; Q53R22;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Frizzled-5;
DE Short=Fz-5;
DE Short=hFz5;
DE AltName: Full=FzE5;
DE Flags: Precursor;
GN Name=FZD5; Synonyms=C2orf31;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8626800; DOI=10.1074/jbc.271.8.4468;
RA Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J.,
RA Copeland N.G., Jenkins N.A., Nathans J.;
RT "A large family of putative transmembrane receptors homologous to the
RT product of the Drosophila tissue polarity gene frizzled.";
RL J. Biol. Chem. 271:4468-4476(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11408929; DOI=10.3892/ijo.19.1.105;
RA Saitoh T., Hirai M., Katoh M.;
RT "Molecular cloning and characterization of human Frizzled-5 gene on
RT chromosome 2q33.3-q34 region.";
RL Int. J. Oncol. 19:105-110(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 273-331.
RC TISSUE=Esophageal carcinoma;
RX PubMed=9707618; DOI=10.1073/pnas.95.17.10164;
RA Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.;
RT "A novel frizzled gene identified in human esophageal carcinoma mediates
RT APC/beta-catenin signals.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998).
RN [6]
RP FUNCTION, AND COUPLING TO BETA-CATENIN PATHWAY.
RX PubMed=9054360; DOI=10.1126/science.275.5306.1652;
RA He X., Saint-Jeannet J.P., Wang Y., Nathans J., Dawid I., Varmus H.;
RT "A member of the Frizzled protein family mediating axis induction by Wnt-
RT 5A.";
RL Science 275:1652-1654(1997).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10097073; DOI=10.1073/pnas.96.7.3546;
RA Hsieh J.C., Rattner A., Smallwood P.M., Nathans J.;
RT "Biochemical characterization of Wnt-frizzled interactions using a soluble,
RT biologically active vertebrate Wnt protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3546-3551(1999).
RN [8]
RP INTERACTION WITH WNT2B.
RX PubMed=12490564; DOI=10.1242/dev.00244;
RA Kubo F., Takeichi M., Nakagawa S.;
RT "Wnt2b controls retinal cell differentiation at the ciliary marginal
RT zone.";
RL Development 130:587-598(2003).
RN [9]
RP INTERACTION WITH WNT7A.
RX PubMed=18230341; DOI=10.1016/j.bbrc.2008.01.088;
RA Carmon K.S., Loose D.S.;
RT "Wnt7a interaction with Fzd5 and detection of signaling activation using a
RT split eGFP.";
RL Biochem. Biophys. Res. Commun. 368:285-291(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH WNT7A.
RX PubMed=20530549; DOI=10.1242/dev.046722;
RA Sahores M., Gibb A., Salinas P.C.;
RT "Frizzled-5, a receptor for the synaptic organizer Wnt7a, regulates
RT activity-mediated synaptogenesis.";
RL Development 137:2215-2225(2010).
RN [11]
RP UBIQUITINATION BY ZNRF3.
RX PubMed=22575959; DOI=10.1038/nature11019;
RA Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H.,
RA Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R., Bouwmeester T.,
RA Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C., Cong F.;
RT "ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive manner.";
RL Nature 485:195-200(2012).
RN [12]
RP UBIQUITINATION BY RNF43.
RX PubMed=22895187; DOI=10.1038/nature11308;
RA Koo B.K., Spit M., Jordens I., Low T.Y., Stange D.E., van de Wetering M.,
RA van Es J.H., Mohammed S., Heck A.J., Maurice M.M., Clevers H.;
RT "Tumour suppressor RNF43 is a stem-cell E3 ligase that induces endocytosis
RT of Wnt receptors.";
RL Nature 488:665-669(2012).
RN [13] {ECO:0007744|PDB:5URY, ECO:0007744|PDB:5URZ}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 28-155 IN COMPLEX WITH
RP UNSATURATED FATTY ACID, SUBUNIT, GLYCOSYLATION AT ASN-47, AND DISULFIDE
RP BONDS.
RX PubMed=28377511; DOI=10.1073/pnas.1618293114;
RA Nile A.H., Mukund S., Stanger K., Wang W., Hannoush R.N.;
RT "Unsaturated fatty acyl recognition by Frizzled receptors mediates
RT dimerization upon Wnt ligand binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:4147-4152(2017).
CC -!- FUNCTION: Receptor for Wnt proteins (PubMed:9054360, PubMed:10097073,
CC PubMed:20530549). Can activate WNT2, WNT10B, WNT5A, but not WNT2B or
CC WNT4 (in vitro); the in vivo situation may be different since not all
CC of these are known to be coexpressed (By similarity). In neurons,
CC activation of WNT7A promotes formation of synapses (PubMed:20530549).
CC Functions in the canonical Wnt/beta-catenin signaling pathway. The
CC canonical Wnt/beta-catenin signaling pathway leads to the activation of
CC disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation
CC of beta-catenin and activation of Wnt target genes (By similarity). A
CC second signaling pathway involving PKC and calcium fluxes has been seen
CC for some family members, but it is not yet clear if it represents a
CC distinct pathway or if it can be integrated in the canonical pathway,
CC as PKC seems to be required for Wnt-mediated inactivation of GSK-3
CC kinase. Both pathways seem to involve interactions with G-proteins. May
CC be involved in transduction and intercellular transmission of polarity
CC information during tissue morphogenesis and/or in differentiated
CC tissues (Probable). Plays a role in yolk sac angiogenesis and in
CC placental vascularization (By similarity).
CC {ECO:0000250|UniProtKB:Q9EQD0, ECO:0000269|PubMed:10097073,
CC ECO:0000269|PubMed:20530549, ECO:0000269|PubMed:9054360, ECO:0000305}.
CC -!- SUBUNIT: Binding of unsaturated fatty acid molecules (via FZ domain)
CC promotes homodimerization (PubMed:28377511). Interacts with WNT2B
CC (PubMed:12490564). Interacts with WNT7A (PubMed:18230341,
CC PubMed:20530549). Interacts with GOPC (By similarity).
CC {ECO:0000250|UniProtKB:Q9EQD0, ECO:0000269|PubMed:12490564,
CC ECO:0000269|PubMed:18230341, ECO:0000269|PubMed:20530549,
CC ECO:0000269|PubMed:28377511}.
CC -!- INTERACTION:
CC Q13467; Q6P3W7: SCYL2; NbExp=4; IntAct=EBI-3913027, EBI-1046810;
CC Q13467; P78383: SLC35B1; NbExp=3; IntAct=EBI-3913027, EBI-12147661;
CC Q13467; M4NKV9: tcdB; Xeno; NbExp=3; IntAct=EBI-3913027, EBI-20596828;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8CHL0};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8CHL0}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9EQD0}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q9EQD0}. Synapse
CC {ECO:0000250|UniProtKB:Q8CHL0}. Perikaryon
CC {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q8CHL0}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q8CHL0}. Note=Localized at the plasma membrane
CC and also found at the Golgi. {ECO:0000250|UniProtKB:Q9EQD0}.
CC -!- DOMAIN: The PDZ-binding motif mediates interaction with GOPC.
CC {ECO:0000250}.
CC -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl
CC (Disheveled) family members and is involved in the activation of the
CC Wnt/beta-catenin signaling pathway. {ECO:0000250}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF43 and ZNRF3, leading to its degradation by
CC the proteasome. {ECO:0000269|PubMed:22575959,
CC ECO:0000269|PubMed:22895187}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; U43318; AAC50385.1; -; mRNA.
DR EMBL; AB043702; BAB60959.1; -; mRNA.
DR EMBL; AK290386; BAF83075.1; -; mRNA.
DR EMBL; AK315338; BAG37738.1; -; mRNA.
DR EMBL; AC096772; AAY24058.1; -; Genomic_DNA.
DR CCDS; CCDS33366.1; -.
DR RefSeq; NP_003459.2; NM_003468.3.
DR PDB; 5URY; X-ray; 2.10 A; A/B=28-155.
DR PDB; 5URZ; X-ray; 2.20 A; A/B=28-155.
DR PDB; 6O39; X-ray; 1.80 A; C=28-150.
DR PDB; 6WW2; EM; 3.70 A; R=27-428, R=441-546.
DR PDBsum; 5URY; -.
DR PDBsum; 5URZ; -.
DR PDBsum; 6O39; -.
DR PDBsum; 6WW2; -.
DR AlphaFoldDB; Q13467; -.
DR SMR; Q13467; -.
DR BioGRID; 113609; 20.
DR CORUM; Q13467; -.
DR IntAct; Q13467; 18.
DR MINT; Q13467; -.
DR STRING; 9606.ENSP00000354607; -.
DR ChEMBL; CHEMBL3559687; -.
DR GuidetoPHARMACOLOGY; 233; -.
DR GlyGen; Q13467; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q13467; -.
DR PhosphoSitePlus; Q13467; -.
DR BioMuta; FZD5; -.
DR DMDM; 116242481; -.
DR EPD; Q13467; -.
DR jPOST; Q13467; -.
DR MassIVE; Q13467; -.
DR MaxQB; Q13467; -.
DR PaxDb; Q13467; -.
DR PeptideAtlas; Q13467; -.
DR PRIDE; Q13467; -.
DR ProteomicsDB; 59463; -.
DR TopDownProteomics; Q13467; -.
DR ABCD; Q13467; 61 sequenced antibodies.
DR Antibodypedia; 19996; 427 antibodies from 36 providers.
DR DNASU; 7855; -.
DR Ensembl; ENST00000295417.4; ENSP00000354607.3; ENSG00000163251.4.
DR GeneID; 7855; -.
DR KEGG; hsa:7855; -.
DR MANE-Select; ENST00000295417.4; ENSP00000354607.3; NM_003468.4; NP_003459.2.
DR UCSC; uc002vcj.4; human.
DR CTD; 7855; -.
DR DisGeNET; 7855; -.
DR GeneCards; FZD5; -.
DR HGNC; HGNC:4043; FZD5.
DR HPA; ENSG00000163251; Tissue enhanced (liver).
DR MalaCards; FZD5; -.
DR MIM; 601723; gene.
DR neXtProt; NX_Q13467; -.
DR OpenTargets; ENSG00000163251; -.
DR Orphanet; 98942; Coloboma of choroid and retina.
DR Orphanet; 98943; Coloboma of eye lens.
DR Orphanet; 98946; Coloboma of eyelid.
DR Orphanet; 98944; Coloboma of iris.
DR Orphanet; 98945; Coloboma of macula.
DR Orphanet; 98947; Coloboma of optic disc.
DR PharmGKB; PA28460; -.
DR VEuPathDB; HostDB:ENSG00000163251; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000162639; -.
DR HOGENOM; CLU_007873_2_0_1; -.
DR InParanoid; Q13467; -.
DR OMA; MARPDPC; -.
DR OrthoDB; 509772at2759; -.
DR PhylomeDB; Q13467; -.
DR TreeFam; TF317907; -.
DR PathwayCommons; Q13467; -.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-HSA-5340588; Signaling by RNF43 mutants.
DR SignaLink; Q13467; -.
DR SIGNOR; Q13467; -.
DR BioGRID-ORCS; 7855; 23 hits in 1082 CRISPR screens.
DR ChiTaRS; FZD5; human.
DR GeneWiki; FZD5; -.
DR GenomeRNAi; 7855; -.
DR Pharos; Q13467; Tbio.
DR PRO; PR:Q13467; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13467; protein.
DR Bgee; ENSG00000163251; Expressed in jejunal mucosa and 174 other tissues.
DR Genevisible; Q13467; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0042813; F:Wnt receptor activity; IDA:FlyBase.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IDA:BHF-UCL.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Ensembl.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IDA:BHF-UCL.
DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; IEA:Ensembl.
DR GO; GO:0000578; P:embryonic axis specification; IDA:BHF-UCL.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0002071; P:glandular epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0060574; P:intestinal epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:BHF-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:ARUK-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0002726; P:positive regulation of T cell cytokine production; IDA:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; IEA:Ensembl.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:1901382; P:regulation of chorionic trophoblast cell proliferation; IEA:Ensembl.
DR GO; GO:0060061; P:Spemann organizer formation; IDA:BHF-UCL.
DR GO; GO:0007416; P:synapse assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0060715; P:syncytiotrophoblast cell differentiation involved in labyrinthine layer development; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR CDD; cd07460; CRD_FZ5; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR037441; FZ5_CRD.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR Pfam; PF01534; Frizzled; 1.
DR Pfam; PF01392; Fz; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM00063; FRI; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Developmental protein;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Golgi apparatus;
KW Lipid-binding; Membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Wnt signaling pathway.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..585
FT /note="Frizzled-5"
FT /id="PRO_0000012990"
FT TOPO_DOM 27..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..500
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..150
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 156..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 525..530
FT /note="Lys-Thr-X-X-X-Trp motif, mediates interaction with
FT the PDZ domain of Dvl family members"
FT /evidence="ECO:0000250"
FT MOTIF 583..585
FT /note="PDZ-binding"
FT COMPBIAS 160..177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28377511,
FT ECO:0007744|PDB:5URY, ECO:0007744|PDB:5URZ"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:28377511, ECO:0007744|PDB:5URY,
FT ECO:0007744|PDB:5URZ"
FT DISULFID 41..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:28377511, ECO:0007744|PDB:5URY,
FT ECO:0007744|PDB:5URZ"
FT DISULFID 78..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:28377511, ECO:0007744|PDB:5URY,
FT ECO:0007744|PDB:5URZ"
FT DISULFID 105..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:28377511, ECO:0007744|PDB:5URY,
FT ECO:0007744|PDB:5URZ"
FT DISULFID 109..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090,
FT ECO:0000269|PubMed:28377511, ECO:0007744|PDB:5URY,
FT ECO:0007744|PDB:5URZ"
FT VARIANT 216
FT /note="P -> L (in dbSNP:rs35994626)"
FT /id="VAR_049291"
FT CONFLICT 88
FT /note="S -> T (in Ref. 1; AAC50385)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..263
FT /note="ER -> DT (in Ref. 1; AAC50385)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="G -> A (in Ref. 1; AAC50385)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="A -> G (in Ref. 1; AAC50385)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="D -> G (in Ref. 4; BAF83075)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="G -> R (in Ref. 1; AAC50385)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="M -> V (in Ref. 4; BAG37738)"
FT /evidence="ECO:0000305"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6O39"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:6O39"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6O39"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:6O39"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:6O39"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:6O39"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6O39"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6O39"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6O39"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6O39"
SQ SEQUENCE 585 AA; 64507 MW; AC3AB2CD912C1B0A CRC64;
MARPDPSAPP SLLLLLLAQL VGRAAAASKA PVCQEITVPM CRGIGYNLTH MPNQFNHDTQ
DEAGLEVHQF WPLVEIQCSP DLRFFLCSMY TPICLPDYHK PLPPCRSVCE RAKAGCSPLM
RQYGFAWPER MSCDRLPVLG RDAEVLCMDY NRSEATTAPP RPFPAKPTLP GPPGAPASGG
ECPAGGPFVC KCREPFVPIL KESHPLYNKV RTGQVPNCAV PCYQPSFSAD ERTFATFWIG
LWSVLCFIST STTVATFLID MERFRYPERP IIFLSACYLC VSLGFLVRLV VGHASVACSR
EHNHIHYETT GPALCTIVFL LVYFFGMASS IWWVILSLTW FLAAGMKWGN EAIAGYAQYF
HLAAWLIPSV KSITALALSS VDGDPVAGIC YVGNQNLNSL RGFVLGPLVL YLLVGTLFLL
AGFVSLFRIR SVIKQGGTKT DKLEKLMIRI GIFTLLYTVP ASIVVACYLY EQHYRESWEA
ALTCACPGHD TGQPRAKPEY WVLMLKYFMC LVVGITSGVW IWSGKTVESW RRFTSRCCCR
PRRGHKSGGA MAAGDYPEAS AALTGRTGPP GPAATYHKQV SLSHV
